The amphiphilic character of glycogenin.

Abstract:

:This study describes for the first time the amphiphilicity of the protein moiety of proteoglycogen. Glycogenin but not proteoglycogen associates to phospholipid vesicles and forms by itself stable Gibbs and Langmuir monolayers at the air-buffer interface. The adsorption free energy (-6.7 kcal/mol) and the glycogenin collapse pressure (47 mN/m) are indicative of its high surface activity which can thermodynamically drive and retain the protein at the membrane interface to a maximum equilibrium adsorption surface pressure of 21 mN/m. The marked surface activity of glycogenin is further enhanced by its thermodynamically favorable penetration into zwitterionic and anionic phospholipids with a high cut-off surface pressure point above 30 mN/m. The strong association to phospholipid vesicles and the marked surface activity of glycogenin correspond to a high amphiphilic character which supports its spontaneous association to membrane interfaces, in which the de novo biosynthesis of glycogen was proposed to initiate.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Carrizo ME,Miozzo MC,Maggio B,Curtino JA

doi

10.1016/s0014-5793(01)03192-1

keywords:

subject

Has Abstract

pub_date

2001-12-07 00:00:00

pages

323-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)03192-1

journal_volume

509

pub_type

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